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Journal of Analytical Chemistry

, Volume 65, Issue 13, pp 1320–1327 | Cite as

New cysteine-modifying reagents: Efficiency of derivatization and influence on the signals of the protonated molecules of disulfide-containing peptides in matrix-assisted laser desorption/ionization mass spectrometry

  • T. Yu. Samgina
  • V. A. Gorshkov
  • E. A. Vorontsov
  • V. V. Bagrov
  • I. E. Nifant’ev
  • A. T. LebedevEmail author
Articles

Abstract

Mass spectrometric de novo sequencing of skin secretion peptides from genus Rana is complicated because of C-terminal disulfide cycles present in their structure. Brevinin-1E and brevinin-2Ec from the skin secretion of the Marsh Frog R. ridibunda were used for a comparative study of six N-phenylmaleimide derivatives as new alkylating agents for cysteine thiol moieties. The paper describes the synthesis and confirmation of the structures of the obtained compounds. A procedure was developed for modifying thiol groups with the proposed reagents. Alkylation efficiency and the effect on the peak intensity in matrix-assisted laser desorption/ionization (MALDI) spectra were investigated. The best results were obtained for 2,4- and 2,5-dimethylphenylmaleimides. Additionally tested iodoacetic acid was shown to be a powerful modifier of thiol groups, while its excess notably increases the intensities of the peaks of protonated molecules in the MALDI mass spectra of both peptides.

Keywords

disulfide-containing peptides alkylation cysteine N-phenylmaleimide MALDI-TOF iodoacetic acid 

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Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • T. Yu. Samgina
    • 1
  • V. A. Gorshkov
    • 1
  • E. A. Vorontsov
    • 1
  • V. V. Bagrov
    • 1
  • I. E. Nifant’ev
    • 1
  • A. T. Lebedev
    • 1
    Email author
  1. 1.Faculty of ChemistryMoscow State UniversityMoscowRussia

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